BMRB Entry 17357
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17357
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Title: PsbQ protein PubMed: 21259076
Deposition date: 2010-12-13 Original release date: 2011-02-01
Authors: Hornicakova, Michaela; Muller, Norbert
Citation: Horniakova, Michaela; Kohoutova, Jaroslava; Schlagnitweit, Judith; Wohlschlager, Christian; Ettrich, Rudiger; Fiala, Radovan; Schoefberger, Wolfgang; Muller, Norbert. "Backbone assignment and secondary structure of the PsbQ protein from photosystem II." Biomol. NMR Assignments 5, 169-175 (2011).
Assembly members:
PsbQ_protein, polymer, 149 residues, Formula weight is not available
Natural source: Common Name: spinach Taxonomy ID: 3562 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Spinacea oleracea
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PsbQ_protein: EARPIVVGPPPPLSGGLPGT
ENSDQARDGTLPYTKDRFYL
QPLPPTEAAQRAKVSASEIL
NVKQFIDRKAWPSLQNDLRL
RASYLRYDLKTVISAKPKDE
KKSLQELTSKLFSSIDNLDH
AAKIKSPTEAEKYYGQTVSN
INEVLAKLG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 401 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 448 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PsbQ | 1 |
Entities:
Entity 1, PsbQ 149 residues - Formula weight is not available
| 1 | GLU | ALA | ARG | PRO | ILE | VAL | VAL | GLY | PRO | PRO | ||||
| 2 | PRO | PRO | LEU | SER | GLY | GLY | LEU | PRO | GLY | THR | ||||
| 3 | GLU | ASN | SER | ASP | GLN | ALA | ARG | ASP | GLY | THR | ||||
| 4 | LEU | PRO | TYR | THR | LYS | ASP | ARG | PHE | TYR | LEU | ||||
| 5 | GLN | PRO | LEU | PRO | PRO | THR | GLU | ALA | ALA | GLN | ||||
| 6 | ARG | ALA | LYS | VAL | SER | ALA | SER | GLU | ILE | LEU | ||||
| 7 | ASN | VAL | LYS | GLN | PHE | ILE | ASP | ARG | LYS | ALA | ||||
| 8 | TRP | PRO | SER | LEU | GLN | ASN | ASP | LEU | ARG | LEU | ||||
| 9 | ARG | ALA | SER | TYR | LEU | ARG | TYR | ASP | LEU | LYS | ||||
| 10 | THR | VAL | ILE | SER | ALA | LYS | PRO | LYS | ASP | GLU | ||||
| 11 | LYS | LYS | SER | LEU | GLN | GLU | LEU | THR | SER | LYS | ||||
| 12 | LEU | PHE | SER | SER | ILE | ASP | ASN | LEU | ASP | HIS | ||||
| 13 | ALA | ALA | LYS | ILE | LYS | SER | PRO | THR | GLU | ALA | ||||
| 14 | GLU | LYS | TYR | TYR | GLY | GLN | THR | VAL | SER | ASN | ||||
| 15 | ILE | ASN | GLU | VAL | LEU | ALA | LYS | LEU | GLY |
Samples:
sample_1: PsbQ protein, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.00; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C detected CBCACON | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C detected CBCANCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C detected CON | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking
TOPSPIN v2.1, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 750 MHz
- Bruker DRX 600 MHz
- Bruker Avance 600 MHz
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts